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Literature summary extracted from

  • Yuan, S.; Jiang, W.; Chen, L.; Guo, Y.; Liu, Z.
    A novel serine hydroxymethyltransferase from marine bacterium Alcanivorax sp. and its application on enzymatic synthesis of L-serine (2014), J. Mol. Catal. B, 109, 17-23.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 gene glyA, DNa and amino acid sequence determination and analysis, subcloning in Escherichia coli strain DH5alpha, sequence comparison, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3) Alcanivorax sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.1 Cu2+ strong inhibition Alcanivorax sp.
2.1.2.1 SDS strong inhibition Alcanivorax sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.2.1 additional information Mg2+, K+, Na+and EDTA have no significant effect on the enzyme activity Alcanivorax sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.2.1 45200
-
x * 45200, about, sequence calculation, recombinant enzyme, SDS-PAGE Alcanivorax sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Alcanivorax sp.
-
tetrahydrofolate + L-serine
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Alcanivorax sp.
-
gene glyA
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Alcanivorax sp. tetrahydrofolate + L-serine
-
r
2.1.2.1 additional information the enzyme is also active with DL-threo-3-phenylserine Alcanivorax sp. ?
-
?

Subunits

EC Number Subunits Comment Organism
2.1.2.1 ? x * 45200, about, sequence calculation, recombinant enzyme, SDS-PAGE Alcanivorax sp.

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 serine hydroxymethyltransferase
-
Alcanivorax sp.
2.1.2.1 SHMT
-
Alcanivorax sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.2.1 50
-
-
Alcanivorax sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.2.1 30 60 activity range, profile overview Alcanivorax sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.1 7
-
-
Alcanivorax sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.2.1 5.5 9.5 activity range, profile overview Alcanivorax sp.

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.2.1 6 8 purified recombinant enzyme, over 60% maximal activity remains after 24 h at pH 6.0-7.5, 4°C, less than 20% of maximal activity at pH 8.0 Alcanivorax sp.

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 5,10-methylenetetrahydrofolate
-
Alcanivorax sp.
2.1.2.1 pyridoxal 5'-phosphate dependent on Alcanivorax sp.
2.1.2.1 tetrahydrofolate
-
Alcanivorax sp.